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Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Thermotoga neapolitana
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

pH dependencei

Optimum pH is 5.5-6.

Temperature dependencei

Optimum temperature is 102 degrees Celsius. Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei498 – 4981Proton donorBy similarity
Active sitei604 – 6041NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Endoxylanase
Gene namesi
Name:xynA
OrganismiThermotoga neapolitana
Taxonomic identifieri2337 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 10551026Endo-1,4-beta-xylanase APRO_0000007987Add
BLAST

Proteomic databases

PRIDEiQ60042.

Structurei

3D structure databases

ProteinModelPortaliQ60042.
SMRiQ60042. Positions 867-1055.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini720 – 851132CBM-cenC 1Add
BLAST
Domaini895 – 1040146CBM-cenC 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 367338AAdd
BLAST
Regioni371 – 687317B, catalyticAdd
BLAST

Domaini

The C-terminal CBM-CenC domains mediate the binding of XynA to microcrystalline cellulose. CBM-CenC 2 alone can also promote cellulose binding (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60042-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRKKRRGFLN ASTAVLVGIL AGFLGVVLAA TGALGFAVRE SLLLKQFLFL
60 70 80 90 100
SFEGNTDGAS PFGKDVVVTA SQDVAADGEY SLKVENRTSV WDGVEIDLTG
110 120 130 140 150
KVNTGTDYLL SFHVYQTSDS PQLFSVLART EDEKGERYKI LADKVVVPNY
160 170 180 190 200
WKEILVPFSP TFEGTPAKFS LIITSPKKTD FVFYVDNVQV LTPKEAGPKV
210 220 230 240 250
VYETSFEKGI GDWQPRGSDV KISISPKVAH SGKKSLFVSN RQKGWHGAQI
260 270 280 290 300
SLKGILKTGK TYAFEAWVYQ ESGQDQTIIM TMQRKYSSDS STKYEWIKAA
310 320 330 340 350
TVPSGQWVQL SGTYTIPAGV TVEDLTLYFE SQNPTLEFYV DDVKVVDTTS
360 370 380 390 400
AEIKLEMNPE EEIPALKDVL KDYFRVGVAL PSKVFINQKD IALISKHSNS
410 420 430 440 450
STAENEMKPD SLLAGIENGK LKFRFETADK YIEFAQQNGM VVRGHTLVWH
460 470 480 490 500
NQTPEWFFKD ENGNLLSKEE MTERLREYIH TVVGHFKGKV YAWDVVNEAV
510 520 530 540 550
DPNQPDGLRR STWYQIMGPD YIELAFKFAR EADPNAKLFY NDYNTFEPKK
560 570 580 590 600
RDIIYNLVKS LKEKGLIDGI GMQCHISLAT DIRQIEEAIK KFSTIPGIEI
610 620 630 640 650
HITELDISVY RDSTSNYSEA PRTALIEQAH KMAQLFKIFK KYSNVITNVT
660 670 680 690 700
FWGLKDDYSW RATRRNDWPL IFDKDYQAKL AYWAIVAPEV LPPLPKESKI
710 720 730 740 750
SEGEAVVVGM MDDSYMMSKP IEIYDEEGNV KATIRAIWKD STIYVYGEVQ
760 770 780 790 800
DATKKPAEDG VAIFINPNNE RTPYLQPDDT YVVLWTNWKS EVNREDVEVK
810 820 830 840 850
KFVGPGFRRY SFEMSITIPG VEFKKDSYIG FDVAVIDDGK WYSWSDTTNS
860 870 880 890 900
QKTNTMNYGT LKLEGVMVAT AKYGTPVIDG EIDDIWNTTE EIETKSVAMG
910 920 930 940 950
SLEKNATAKV RVLWDEENLY VLAIVKDPVL NKDNSNPWEQ DSVEIFIDEN
960 970 980 990 1000
NHKTGYYEDD DAQFRVNYMN EQSFGTGASA ARFKTAVKLI EGGYIVEAAI
1010 1020 1030 1040 1050
KWKTIKPSPN TVIGFNVQVN DANEKGQRVG IISWSDPTNN SWRDPSKFGN

LRLIK
Length:1,055
Mass (Da):119,323
Last modified:November 1, 1997 - v1
Checksum:iF939845878B87468
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46945 Genomic DNA. Translation: CAA87069.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46945 Genomic DNA. Translation: CAA87069.1.

3D structure databases

ProteinModelPortaliQ60042.
SMRiQ60042. Positions 867-1055.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Proteomic databases

PRIDEiQ60042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant."
    Zverlov V., Piotukh K., Dakhova O., Velikodvorskaya G., Borriss R.
    Appl. Microbiol. Biotechnol. 45:245-247(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Z2706-MC24.

Entry informationi

Entry nameiXYNA_THENE
AccessioniPrimary (citable) accession number: Q60042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 1, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.